7PNQ
Human coronavirus OC43 spike glycoprotein ectodomain in complex with the 43E6 antibody Fab fragment
Summary for 7PNQ
| Entry DOI | 10.2210/pdb7pnq/pdb |
| EMDB information | 13550 |
| Descriptor | 43E6 antibody heavy chain, 43E6 antibody light chain, Spike glycoprotein, ... (4 entities in total) |
| Functional Keywords | coronavirus, glycoprotein, antibody, spike, viral protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 9 |
| Total formula weight | 517433.75 |
| Authors | Hurdiss, D.L. (deposition date: 2021-09-07, release date: 2022-04-20, Last modification date: 2022-11-09) |
| Primary citation | Wang, C.,Hesketh, E.L.,Shamorkina, T.M.,Li, W.,Franken, P.J.,Drabek, D.,van Haperen, R.,Townend, S.,van Kuppeveld, F.J.M.,Grosveld, F.,Ranson, N.A.,Snijder, J.,de Groot, R.J.,Hurdiss, D.L.,Bosch, B.J. Antigenic structure of the human coronavirus OC43 spike reveals exposed and occluded neutralizing epitopes. Nat Commun, 13:2921-2921, 2022 Cited by PubMed Abstract: Human coronavirus OC43 is a globally circulating common cold virus sustained by recurrent reinfections. How it persists in the population and defies existing herd immunity is unknown. Here we focus on viral glycoprotein S, the target for neutralizing antibodies, and provide an in-depth analysis of its antigenic structure. Neutralizing antibodies are directed to the sialoglycan-receptor binding site in S1 domain, but, remarkably, also to S1. The latter block infection yet do not prevent sialoglycan binding. While two distinct neutralizing S1 epitopes are readily accessible in the prefusion S trimer, other sites are occluded such that their accessibility must be subject to conformational changes in S during cell-entry. While non-neutralizing antibodies were broadly reactive against a collection of natural OC43 variants, neutralizing antibodies generally displayed restricted binding breadth. Our data provide a structure-based understanding of protective immunity and adaptive evolution for this endemic coronavirus which emerged in humans long before SARS-CoV-2. PubMed: 35614127DOI: 10.1038/s41467-022-30658-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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